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DTSTAMP:20260414T234526
DTSTART:20141106T113000
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URL:https://murmitoyen.com/events/vanille/udem/detail/513193
LOCATION:Université de Montréal - Pavillon J.-Armand-Bombardier\, 5155\, 
 chemin de la rampe \, Montréal\, QC\, Canada\, H3T 2B2
SUMMARY:Conférence de Pratul Agarwal\, Ph.D. (Oak Ridge)
DESCRIPTION:Titre : Conformational Diversity and Its Roal Enzyme Catalysis.
 Endroit : Pavilllon J.-A.-Bombardier\, salle 1035 à 11 h 30Hôte : Profes
 seure Joelle PelletierLa conférence sera prononcée en anglais par le che
 rcheur Pratuel Agarwal\, Ph.D. du Oak Ridge National Laboratory au Tenness
 ee. Elle est commanditée par l'INRS-Institut Armand-Frappier.Résumé : 
 Proteins are not rigid objects and they are constantly undergoing fluctuat
 ions. Evidence from an increasing number of investigations indicate that i
 nternal motions of proteins play a role in the designated function. Intern
 al motions driven by temperature and the surrounding environment enable en
 zymes to sample conformational diversity formed by a hierarchy of conforma
 tional sub-states. A small number of these conformational states contain t
 he functionally structural features for enzyme systems. The low population
 s in these states makes it difficult to obtain structural and dynamical in
 formation. We have developed methodology to accurately identify these stat
 es and in combination with neutron scattering and NMR investigations\, com
 putational simulations are being used to identify and more importantly qua
 ntify the populations in these functionally relevant conformational sub-st
 ates. These joint experimental-computational strategy has already provided
  insights into a number of enzyme systems including dihydrofolate reductas
 e and ribonuclease A. Results from these and other enzyme systems will be 
 presented. Overall\, these hybrid methods provide a unique opportunity for
  investigating the conformational diversity of proteins and obtain quantit
 ative information regarding the role of protein and solvent dynamics in en
 zyme catalysis.Références : 1)  Ramanathan\, A.\; Savol\, A.\; Burger\,
  V.\; Chennubhotla\, C. S.*\; Agarwal\, P. K.* Protein Conformational Popu
 lations and Functionally Relevant Sub-states\, Accounts of Chemical Resear
 ch (2014)\, 47(1) \, 149-156.   2) Ramanathan\, A.\; Savol\, A.\; Langmea
 d\, C. J.\; Agarwal\, P. K.*\; Chennubhotla\, C. S.* Discovering conformat
 ional sub-states relevant to protein function\, PLoS ONE (2011) 6(1): e158
 27.3) Ramanathan\, A.\; Agarwal\, P. K.* Evolutionarily Conserved Linkage 
 between Enzyme Fold\, Flexibility\, and Catalysis\, PLoS Biology (2011)\, 
 9(11)\, e1001193. Information supplémentaireAnnonce PDF de la conférence
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